MFS55_MYCTA
ID MFS55_MYCTA Reviewed; 518 AA.
AC A5U2B2;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Probable triacylglyceride transporter MRA_1419 {ECO:0000250|UniProtKB:P9WJY3};
DE AltName: Full=MFS-type drug efflux transporter P55;
GN OrderedLocusNames=MRA_1419;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=25356793; DOI=10.1371/journal.ppat.1004471;
RA Shukla S., Richardson E.T., Athman J.J., Shi L., Wearsch P.A., McDonald D.,
RA Banaei N., Boom W.H., Jackson M., Harding C.V.;
RT "Mycobacterium tuberculosis lipoprotein LprG binds lipoarabinomannan and
RT determines its cell envelope localization to control phagolysosomal
RT fusion.";
RL PLoS Pathog. 10:E1004471-E1004471(2014).
CC -!- FUNCTION: In association with lipoprotein LprG probably transports
CC triacylglycerides (TAG) across the inner cell membrane into the
CC periplasm; TAG probably regulates lipid metabolism and growth
CC regulation. May be an efflux transporter and involved in maintaining
CC correct cell wall permeability (By similarity). Probably required with
CC LprG for normal surface localization of lipoarabinomannan (LAM)
CC (PubMed:25356793). {ECO:0000250|UniProtKB:P9WJY3,
CC ECO:0000305|PubMed:25356793}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Single lprG deletion mutant (probably does not
CC express this protein) has decreased surface-exposed glycolipid
CC lipoarabinomannan (LAM), although cellular LAM, LM and PIM content is
CC normal (PubMed:25356793). {ECO:0000269|PubMed:25356793}.
CC -!- MISCELLANEOUS: Bacterial LAM blocks host cell phagosome-lysosome fusion
CC and is one way in which M.tuberculosis evades the host immune system.
CC {ECO:0000305|PubMed:25356793}.
CC -!- MISCELLANEOUS: Triacylglycerides accumulate in lipid droplets in the
CC cytoplasm of M.tuberculosis stationary phase and dormant bacteria, and
CC are used as an energy source during starvation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; CP000611; ABQ73162.1; -; Genomic_DNA.
DR RefSeq; WP_003407310.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U2B2; -.
DR SMR; A5U2B2; -.
DR STRING; 419947.MRA_1419; -.
DR EnsemblBacteria; ABQ73162; ABQ73162; MRA_1419.
DR GeneID; 45425388; -.
DR KEGG; mra:MRA_1419; -.
DR eggNOG; COG0477; Bacteria.
DR HOGENOM; CLU_000960_2_5_11; -.
DR OMA; AGYWMTP; -.
DR OrthoDB; 1108236at2; -.
DR Proteomes; UP000001988; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..518
FT /note="Probable triacylglyceride transporter MRA_1419"
FT /id="PRO_0000391007"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 518 AA; 54689 MW; 3D211E3F5A3F77D0 CRC64;
MRAGRRVAIS AGSLAVLLGA LDTYVVVTIM RDIMNSVGIP INQLHRITWI VTMYLLGYIA
AMPLLGRASD RFGRKLMLQV SLAGFIIGSV VTALAGHFGD FHMLIAGRTI QGVASGALLP
ITLALGADLW SQRNRAGVLG GIGAAQELGS VLGPLYGIFI VWLLHDWRDV FWINVPLTAI
AMVMIHFSLP SHDRSTEPER VDLVGGLLLA LALGLAVIGL YNPNPDGKHV LPDYGAPLLV
GALVAAVAFF GWERFARTRL IDPAGVHFRP FLSALGASVA AGAALMVTLV DVELFGQGVL
QMDQAQAAGM LLWFLIALPI GAVTGGWIAT RAGDRAVAFA GLLIAAYGYW LISHWPVDLL
ADRHNILGLF TVPAMHTDLV VAGLGLGLVI GPLSSATLRV VPSAQHGIAS AAVVVARMTG
MLIGVAALSA WGLYRFNQIL AGLSAAIPPN ASLLERAAAI GARYQQAFAL MYGEIFTITA
IVCVFGAVLG LLISGRKEHA DEPEVQEQPT LAPQVEPL
